DDX41_HUMAN
ID DDX41_HUMAN Reviewed; 622 AA.
AC Q9UJV9; B2RDC8; Q96BK6; Q96K05; Q9NT96; Q9NW04;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX41;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 41;
DE AltName: Full=DEAD box protein abstrakt homolog;
GN Name=DDX41; Synonyms=ABS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10607561; DOI=10.1016/s0960-9822(00)80082-2;
RA Irion U., Leptin M.;
RT "Developmental and cell biological functions of the Drosophila DEAD-box
RT protein abstrakt.";
RL Curr. Biol. 9:1373-1381(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-622.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-23, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-23, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-21 AND SER-23, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP INVOLVEMENT IN MPLPF, VARIANTS MPLPF THR-396 AND HIS-525, CHARACTERIZATION
RP OF VARIANT MPLPF HIS-525, FUNCTION, AND SUBUNIT.
RX PubMed=25920683; DOI=10.1016/j.ccell.2015.03.017;
RA Polprasert C., Schulze I., Sekeres M.A., Makishima H., Przychodzen B.,
RA Hosono N., Singh J., Padgett R.A., Gu X., Phillips J.G., Clemente M.,
RA Parker Y., Lindner D., Dienes B., Jankowsky E., Saunthararajah Y., Du Y.,
RA Oakley K., Nguyen N., Mukherjee S., Pabst C., Godley L.A., Churpek J.E.,
RA Pollyea D.A., Krug U., Berdel W.E., Klein H.U., Dugas M., Shiraishi Y.,
RA Chiba K., Tanaka H., Miyano S., Yoshida K., Ogawa S., Mueller-Tidow C.,
RA Maciejewski J.P.;
RT "Inherited and Somatic Defects in DDX41 in Myeloid Neoplasms.";
RL Cancer Cell 27:658-670(2015).
RN [16]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [17]
RP INVOLVEMENT IN MPLPF, VARIANTS MPLPF TRP-164 AND HIS-525, CHARACTERIZATION
RP OF VARIANTS MPLPF TRP-164 AND HIS-525, AND SUBCELLULAR LOCATION.
RX PubMed=26712909; DOI=10.1182/blood-2015-10-676098;
RA Lewinsohn M., Brown A.L., Weinel L.M., Phung C., Rafidi G., Lee M.K.,
RA Schreiber A.W., Feng J., Babic M., Chong C.E., Lee Y., Yong A.,
RA Suthers G.K., Poplawski N., Altree M., Phillips K., Jaensch L., Fine M.,
RA D'Andrea R.J., Lewis I.D., Medeiros B.C., Pollyea D.A., King M.C.,
RA Walsh T., Keel S., Shimamura A., Godley L.A., Hahn C.N., Churpek J.E.,
RA Scott H.S.;
RT "Novel germ line DDX41 mutations define families with a lower age of
RT MDS/AML onset and lymphoid malignancies.";
RL Blood 127:1017-1023(2016).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-416 AND LYS-442, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [19]
RP INTERACTION WITH FAM50A.
RX PubMed=32703943; DOI=10.1038/s41467-020-17452-6;
RA Lee Y.R., Khan K., Armfield-Uhas K., Srikanth S., Thompson N.A., Pardo M.,
RA Yu L., Norris J.W., Peng Y., Gripp K.W., Aleck K.A., Li C., Spence E.,
RA Choi T.I., Kwon S.J., Park H.M., Yu D., Do Heo W., Mooney M.R., Baig S.M.,
RA Wentzensen I.M., Telegrafi A., McWalter K., Moreland T., Roadhouse C.,
RA Ramsey K., Lyons M.J., Skinner C., Alexov E., Katsanis N., Stevenson R.E.,
RA Choudhary J.S., Adams D.J., Kim C.H., Davis E.E., Schwartz C.E.;
RT "Mutations in FAM50A suggest that Armfield XLID syndrome is a
RT spliceosomopathy.";
RL Nat. Commun. 11:3698-3698(2020).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 402-569.
RX PubMed=20941364; DOI=10.1371/journal.pone.0012791;
RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M.,
RA Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M.,
RA Thorsell A.G., Schuler H.;
RT "Comparative structural analysis of human DEAD-box RNA helicases.";
RL PLoS ONE 5:E12791-E12791(2010).
CC -!- FUNCTION: Probable ATP-dependent RNA helicase. Is required during post-
CC transcriptional gene expression. May be involved in pre-mRNA splicing.
CC {ECO:0000269|PubMed:25920683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638,
CC PubMed:25920683). Interacts with ERCC6 (PubMed:26030138). Interacts
CC with FAM50A (PubMed:32703943). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:25920683, ECO:0000269|PubMed:26030138,
CC ECO:0000269|PubMed:32703943}.
CC -!- INTERACTION:
CC Q9UJV9; Q96BJ3: AIDA; NbExp=3; IntAct=EBI-1046350, EBI-4401674;
CC Q9UJV9; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-1046350, EBI-739624;
CC Q9UJV9; P42858: HTT; NbExp=6; IntAct=EBI-1046350, EBI-466029;
CC Q9UJV9; Q8N5F7: NKAP; NbExp=3; IntAct=EBI-1046350, EBI-721539;
CC Q9UJV9; Q5M9Q1: NKAPL; NbExp=5; IntAct=EBI-1046350, EBI-11423380;
CC Q9UJV9; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-1046350, EBI-747107;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26712909}.
CC -!- DISEASE: Myeloproliferative/lymphoproliferative neoplasms, familial
CC (MPLPF) [MIM:616871]: A familial cancer predisposition syndrome with
CC incomplete penetrance, characterized by increased susceptibility to
CC myeloid neoplasms and rarely to lymphoid malignancies. MPLPF
CC inheritance is autosomal dominant. {ECO:0000269|PubMed:25920683,
CC ECO:0000269|PubMed:26712909}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX41 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE46035.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF195417; AAF04150.1; -; mRNA.
DR EMBL; AK001255; BAA91585.1; -; mRNA.
DR EMBL; AK027768; BAB55355.1; -; mRNA.
DR EMBL; AK315491; BAG37875.1; -; mRNA.
DR EMBL; CH471195; EAW84981.1; -; Genomic_DNA.
DR EMBL; BC015476; AAH15476.1; -; mRNA.
DR EMBL; AL137455; CAB70746.1; -; mRNA.
DR EMBL; BX641072; CAE46035.1; ALT_SEQ; mRNA.
DR CCDS; CCDS4427.1; -.
DR PIR; T46269; T46269.
DR RefSeq; NP_001308661.1; NM_001321732.1.
DR RefSeq; NP_001308759.1; NM_001321830.1.
DR RefSeq; NP_057306.2; NM_016222.3.
DR PDB; 2P6N; X-ray; 2.60 A; A/B=402-569.
DR PDB; 5GVR; X-ray; 1.50 A; A=169-402.
DR PDB; 5GVS; X-ray; 2.20 A; A/B/C/D=169-399.
DR PDB; 5H1Y; X-ray; 2.26 A; A/B=153-410.
DR PDBsum; 2P6N; -.
DR PDBsum; 5GVR; -.
DR PDBsum; 5GVS; -.
DR PDBsum; 5H1Y; -.
DR AlphaFoldDB; Q9UJV9; -.
DR SMR; Q9UJV9; -.
DR BioGRID; 119534; 107.
DR CORUM; Q9UJV9; -.
DR IntAct; Q9UJV9; 179.
DR MINT; Q9UJV9; -.
DR STRING; 9606.ENSP00000422753; -.
DR CarbonylDB; Q9UJV9; -.
DR GlyGen; Q9UJV9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UJV9; -.
DR PhosphoSitePlus; Q9UJV9; -.
DR BioMuta; DDX41; -.
DR DMDM; 20532370; -.
DR EPD; Q9UJV9; -.
DR jPOST; Q9UJV9; -.
DR MassIVE; Q9UJV9; -.
DR MaxQB; Q9UJV9; -.
DR PaxDb; Q9UJV9; -.
DR PeptideAtlas; Q9UJV9; -.
DR PRIDE; Q9UJV9; -.
DR ProteomicsDB; 84666; -.
DR Antibodypedia; 17469; 298 antibodies from 31 providers.
DR DNASU; 51428; -.
DR Ensembl; ENST00000330503.12; ENSP00000330349.8; ENSG00000183258.12.
DR GeneID; 51428; -.
DR KEGG; hsa:51428; -.
DR MANE-Select; ENST00000330503.12; ENSP00000330349.8; NM_016222.4; NP_057306.2.
DR UCSC; uc003mho.4; human.
DR CTD; 51428; -.
DR DisGeNET; 51428; -.
DR GeneCards; DDX41; -.
DR GeneReviews; DDX41; -.
DR HGNC; HGNC:18674; DDX41.
DR HPA; ENSG00000183258; Low tissue specificity.
DR MalaCards; DDX41; -.
DR MIM; 608170; gene.
DR MIM; 616871; phenotype.
DR neXtProt; NX_Q9UJV9; -.
DR OpenTargets; ENSG00000183258; -.
DR Orphanet; 488647; DDX41-related hematologic malignancy predisposition syndrome.
DR PharmGKB; PA134908862; -.
DR VEuPathDB; HostDB:ENSG00000183258; -.
DR eggNOG; KOG0341; Eukaryota.
DR GeneTree; ENSGT00940000156333; -.
DR HOGENOM; CLU_003041_16_5_1; -.
DR InParanoid; Q9UJV9; -.
DR OMA; DMLDKKM; -.
DR OrthoDB; 447398at2759; -.
DR PhylomeDB; Q9UJV9; -.
DR TreeFam; TF300340; -.
DR PathwayCommons; Q9UJV9; -.
DR Reactome; R-HSA-1834941; STING mediated induction of host immune responses.
DR Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
DR Reactome; R-HSA-3270619; IRF3-mediated induction of type I IFN.
DR SignaLink; Q9UJV9; -.
DR SIGNOR; Q9UJV9; -.
DR BioGRID-ORCS; 51428; 737 hits in 1084 CRISPR screens.
DR ChiTaRS; DDX41; human.
DR EvolutionaryTrace; Q9UJV9; -.
DR GeneWiki; DDX41; -.
DR GenomeRNAi; 51428; -.
DR Pharos; Q9UJV9; Tbio.
DR PRO; PR:Q9UJV9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UJV9; protein.
DR Bgee; ENSG00000183258; Expressed in granulocyte and 184 other tissues.
DR ExpressionAtlas; Q9UJV9; baseline and differential.
DR Genevisible; Q9UJV9; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0030154; P:cell differentiation; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
DR CDD; cd17951; DEADc_DDX41; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044113; DEADc_DDX41.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Disease variant; Helicase; Hydrolase;
KW Isopeptide bond; Metal-binding; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Spliceosome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..622
FT /note="Probable ATP-dependent RNA helicase DDX41"
FT /id="PRO_0000054970"
FT DOMAIN 212..396
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 407..567
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 580..597
FT /note="CCHC-type"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 181..209
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 344..347
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 33
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91VN6"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 164
FT /note="R -> W (in MPLPF; unknown pathological significance;
FT no effect on localization; dbSNP:rs142143752)"
FT /evidence="ECO:0000269|PubMed:26712909"
FT /id="VAR_076360"
FT VARIANT 396
FT /note="I -> T (in MPLPF; unknown pathological significance;
FT dbSNP:rs747072227)"
FT /evidence="ECO:0000269|PubMed:25920683"
FT /id="VAR_076361"
FT VARIANT 525
FT /note="R -> H (in MPLPF; no effect on localization; changed
FT interaction with spliceosomal complexes;
FT dbSNP:rs869312828)"
FT /evidence="ECO:0000269|PubMed:25920683,
FT ECO:0000269|PubMed:26712909"
FT /id="VAR_076362"
FT CONFLICT 17..43
FT /note="PAGGSRSEAEDEDDEDYVPYVPLRQRR -> LPEEAAPRRKMRTTRTTCPMC
FT RYAAP (in Ref. 1; AAF04150)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="K -> E (in Ref. 2; BAA91585)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="Q -> E (in Ref. 2; BAB55355)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="K -> E (in Ref. 2; BAB55355)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="A -> T (in Ref. 2; BAA91585)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="M -> T (in Ref. 2; BAA91585)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="L -> Q (in Ref. 2; BAB55355)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="D -> G (in Ref. 5; CAE46035)"
FT /evidence="ECO:0000305"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:5H1Y"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:5GVR"
FT TURN 183..187
FT /evidence="ECO:0007829|PDB:5GVR"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:5GVR"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:5GVR"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:5GVR"
FT HELIX 231..249
FT /evidence="ECO:0007829|PDB:5GVR"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:5GVR"
FT HELIX 267..286
FT /evidence="ECO:0007829|PDB:5GVR"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:5GVR"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:5GVR"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:5GVR"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:5GVR"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:5GVR"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:5GVR"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:5H1Y"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:5GVR"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:5GVR"
FT HELIX 380..389
FT /evidence="ECO:0007829|PDB:5GVR"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:5GVR"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:2P6N"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:2P6N"
FT HELIX 420..428
FT /evidence="ECO:0007829|PDB:2P6N"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:2P6N"
FT HELIX 442..455
FT /evidence="ECO:0007829|PDB:2P6N"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:2P6N"
FT HELIX 468..480
FT /evidence="ECO:0007829|PDB:2P6N"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:2P6N"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:2P6N"
FT STRAND 502..508
FT /evidence="ECO:0007829|PDB:2P6N"
FT HELIX 513..520
FT /evidence="ECO:0007829|PDB:2P6N"
FT STRAND 531..536
FT /evidence="ECO:0007829|PDB:2P6N"
FT HELIX 542..554
FT /evidence="ECO:0007829|PDB:2P6N"
FT HELIX 561..564
FT /evidence="ECO:0007829|PDB:2P6N"
SQ SEQUENCE 622 AA; 69838 MW; E0A328724E0DF99A CRC64;
MEESEPERKR ARTDEVPAGG SRSEAEDEDD EDYVPYVPLR QRRQLLLQKL LQRRRKGAAE
EEQQDSGSEP RGDEDDIPLG PQSNVSLLDQ HQHLKEKAEA RKESAKEKQL KEEEKILESV
AEGRALMSVK EMAKGITYDD PIKTSWTPPR YVLSMSEERH ERVRKKYHIL VEGDGIPPPI
KSFKEMKFPA AILRGLKKKG IHHPTPIQIQ GIPTILSGRD MIGIAFTGSG KTLVFTLPVI
MFCLEQEKRL PFSKREGPYG LIICPSRELA RQTHGILEYY CRLLQEDSSP LLRCALCIGG
MSVKEQMETI RHGVHMMVAT PGRLMDLLQK KMVSLDICRY LALDEADRMI DMGFEGDIRT
IFSYFKGQRQ TLLFSATMPK KIQNFAKSAL VKPVTINVGR AGAASLDVIQ EVEYVKEEAK
MVYLLECLQK TPPPVLIFAE KKADVDAIHE YLLLKGVEAV AIHGGKDQEE RTKAIEAFRE
GKKDVLVATD VASKGLDFPA IQHVINYDMP EEIENYVHRI GRTGRSGNTG IATTFINKAC
DESVLMDLKA LLLEAKQKVP PVLQVLHCGD ESMLDIGGER GCAFCGGLGH RITDCPKLEA
MQTKQVSNIG RKDYLAHSSM DF
